Information on EC 1.13.12.2 - lysine 2-monooxygenase

for references in articles please use BRENDA:EC1.13.12.2
Word Map on EC 1.13.12.2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.13.12.2
-
RECOMMENDED NAME
GeneOntology No.
lysine 2-monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-lysine + O2 = 5-aminopentanamide + CO2 + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
oxidative deamination
-
-
oxidative decarboxylation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-lysine degradation IV
-
-
lysine metabolism
-
-
Lysine degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
L-lysine:oxygen 2-oxidoreductase (decarboxylating)
A flavoprotein (FAD). Also acts on other diamino acids.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-22-5
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the bifunctional enzyme L-AAO/MOG belongs to the MAO family of enzymes
malfunction
metabolism
physiological function
-
the enzyme produces 5-aminovalerate, a metabolite of L-lysine catabolism through the aminovalerate pathway in Pseudomonas putida. L-Lysine monooxygenase (DavB) and 5-aminovaleramide amidohydrolase (DavA, EC 3.5.1.30) play key roles in the biotransformation of L-lysine into 5-aminovalerate
additional information
three-dimensional structure of L-AAO/MOG, overview. The key residue for the activity conversion of L-AAO/MOG, Cys254, is located near the aromatic cage (Trp418, Phe473, and Trp516). Cys254 is not directly involved in the substrate binding, but the chemical modification by 4-chloromercuribenzoate or C254I mutation has significant impact on the substrate binding via the side chain of Trp516. A slight difference of the binding position of a substrate dictates the activity of this type of enzyme as oxidase or monooxygenase
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-aminoethylcysteine + O2
?
show the reaction diagram
-
monooxygenase activity
-
-
?
4-chlorolysine + O2
?
show the reaction diagram
-
oxidase activity
-
-
?
4-methyllysine + O2
2-keto-4-methyl-6-amino-n-hexanoate + NH3 + H2O2
show the reaction diagram
-
oxidase activity
-
?
5-hydroxylysine + O2
?
show the reaction diagram
-
oxidase activity
-
-
?
5-methyllysine + O2
4-methyl-5-aminopentanamide + CO2 + H2O
show the reaction diagram
-
monooxygenase activity
-
?
alanine + propylamine + O2
?
show the reaction diagram
-
monooxygenase and oxidase activity
-
-
?
alanine + propylamine + phenazine methosulfate
pyruvate + NH3 + reduced phenazine methosulfate
show the reaction diagram
-
anaerobic conditions, ferricyanide as terminal electron acceptor, dehydrogenase activity
-
?
DL-2,8-diaminooctanoate + O2
2-keto-8-aminooctanoate + NH3 + H2O2
show the reaction diagram
-
oxidase activity
-
-
?
DL-5-hydroxylysine + O2
?
show the reaction diagram
-
monooxygenase activity
-
-
?
DL-7,8-diaminoheptanoate + O2
6-aminohexanamide + CO2 + H2O
show the reaction diagram
-
monooxygenase activity
-
-
?
L-arginine + O2
2-amino-5-guanidinovalerate + NH3 + H2O2
show the reaction diagram
-
oxidase activity
-
-
?
L-arginine + O2
4-guanidinobutanamide + CO2 + H2O
show the reaction diagram
-
-
-
?
L-arginine + O2
4-guanidinobutyramide + CO2 + H2O
show the reaction diagram
L-arginine + phenazine methosulfate
2-keto-5-guanidinovalerate + NH3 + reduced phenazine methosulfate
show the reaction diagram
-
anaerobic conditions, ferricyanide as terminal electron acceptor, dehydrogenase activity
-
?
L-homoarginine + O2
?
show the reaction diagram
-
-
-
-
?
L-lysine + electron acceptor
?
show the reaction diagram
-
anaerobic conditions, electron acceptors are methylene blue, toluylene blue, phenol blue or thymol indophenol
-
-
?
L-lysine + O2
2-keto-6-amino-n-hexanoate + NH3 + H2O2
show the reaction diagram
L-lysine + O2
5-aminopentanamide + CO2 + H2O
show the reaction diagram
L-lysine + O2
5-aminovaleramide + CO2 + H2O
show the reaction diagram
L-Lysine + O2
?
show the reaction diagram
-
L-lysine degradation
-
-
?
L-lysine + phenazine methosulfate
2-keto-6-amino-n-hexanoate + NH3 + reduced phenazine methosulfate
show the reaction diagram
-
anaerobic conditions, ferricyanide as terminal electron acceptor, dehydrogenase activity
-
?
L-ornithine + O2
2-keto-5-amino-n-pentanoate + NH3 + H2O2
show the reaction diagram
-
oxidase activity
-
?
L-ornithine + O2
4-aminobutanamide + CO2 + H2O
show the reaction diagram
-
-
-
?
L-ornithine + phenazine methosulfate
2-keto-5-aminopentanoate + NH3 + reduced phenazine methosulfate
show the reaction diagram
-
anaerobic conditions, ferricyanide as terminal electron acceptor, dehydrogenase activity
-
?
L-thialysine + O2
?
show the reaction diagram
-
monooxygenase and oxidase activity
-
-
?
Nepsilon-methyllysine + O2
5-methylaminopentanamide + CO2 + H2O
show the reaction diagram
-
monooxygenase activity
-
?
threo-4-hydroxy-L-lysine + O2
?
show the reaction diagram
-
oxidase activity
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-lysine + O2
5-aminopentanamide + CO2 + H2O
show the reaction diagram
L-Lysine + O2
?
show the reaction diagram
-
L-lysine degradation
-
-
?
additional information
?
-
W6JQJ6
bifunctional L-amino acid oxidase, EC 1.4.3.2, of Pseudomonas sp. AIU813, renamed as L-amino acid oxidase/monooxygenase (L-AAO/MOG), exhibits L-lysine 2-monooxygenase as well as oxidase activity
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
metals play no role in lysine monooxygenase
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2'-dipyridyl
-
-
2-oxoglutarate
-
60% inhibition at 5 mM
4-Methyllysine
-
at higher substrate concentrations, competitive inhibitor
5-Aminovaleramide
-
42% inhibition at 5 mM
5-Aminovalerate
-
36% inhibition at 5 mM
5-Methyllysine
-
at higher substrate concentrations, competitive inhibitor
8-hydroxyquinoline
-
-
acetate
-
38% inhibition at 5 mM
alkylamines
-
high concentration inhibits, low concentrations stimulate lysine oxygenation
citrate
-
76% inhibition at 5 mM
epsilon-aminocaproate
-
competitive inhibitor toward lysine
glutamate
-
42% inhibition at 5 mM
Glutarate
-
57% inhibition at 5 mM
Nepsilon-Methyllysine
-
at higher substrate concentrations, competitive inhibitor
o-Iodosobenzoate
-
-
ornithine
-
at low concentration of L-lysine reaction is stimulated by L-ornithine, at high concentrations of L-lysine it is inhibited
oxaloacetate
-
67% inhibition at 5 mM
p-chloromercuribenzoate
succinate
-
52% inhibition at 5 mM
Sulfhydryl inhibitors
-
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-Methyllysine
-
at low substrate concentrations
5-Methyllysine
-
at low substrate concentrations
alkylamines
-
low concentrations stimulate lysine oxygenation
KCl
-
activation
NaCl
-
activation
Nepsilon-Methyllysine
-
at low substrate concentrations
ornithine
-
at low concentrations of L-lysine
p-chloromercuribenzoate
-
increases oxidase and dehydrogenase activities, maximal rate of oxidation of lysine at 4-5 mol p-chloromercuribenzoate per mol enzyme, for arginine at 3 mol per mol enzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.125
alanine
-
+ propylamine, oxidation with O2
0.025 - 0.59
arginine
1.35
DL-2,7-diaminoheptanoate
-
monooxygenation
4.1
DL-delta-hydroxylysine
-
monooxygenation
1.8
L-arginine
-
oxidation with O2
0.091 - 0.63
L-lysine
14.5 - 25
L-ornithine
0.33 - 0.67
lysine
0.58 - 0.65
O2
0.25 - 0.42
ornithine
0.018
phenazine methosulfate
-
dehydrogenation of alanine and propylamine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
34.7
L-lysine
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.26
epsilon-aminocaproate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.108
purified recombinant enzyme, pH 7,0, 30C, substrate L-arginine
0.146
purified recombinant enzyme, pH 7,0, 30C, substrate L-ornithine
0.532
purified recombinant enzyme, pH 7,0, 30C, substrate L-lysine
6.1
-
purified recombinant enzyme, pH 7.0, 30C
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
8.5 - 9
-
at low L-lysine concentration
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.4 - 9.4
-
at pH 8.4 about 50% of activity maximum, at pH 9.4 about 40% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
61000
-
4 * 61000, SDS-PAGE
191000
-
sedimentation velocity experiments
246000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 62400, recombinant His-tagged enzyme, SDS-PAGE
tetramer
-
4 * 61000, SDS-PAGE
additional information
three-dimensional structure of L-AAO/MOG, overview. The key residue for the activity conversion of L-AAO/MOG, Cys-254, is located near the aromatic cage (Trp418, Phe473, and Trp516)
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged wild-type and SeMet-labeled enzymes, sitting-drop vapor diffusion method, mixing of 0.001 ml of protein solution, consisting of 20 mg/mL protein in 20 mM HEPES-NaOH, pH 7.6, and 0.001 ml of reservoir solution, consisting of 8% PEG 4000 and 0.1 M Na-acetate, pH 4.6, Se-Met substituted crystals are obtained using reservoir solution consisting of 16% PEG 3350, 0.02 M citric acid, and 0.08 M bis-Tris propane-HCl, pH 8.8, 20C, X-ray diffraction structure determination and analysis at 1.90 and 2.20 A resolution respectively
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
-
4C, several weeks, retains almost full activity
440278
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49
-
inactivation above
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme DavB from Escherichia coli by ncikel affinity chromatography
-
recombinant His-tagged wild-type and and SeMet-labeled enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, anion exchange chromatography, and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene davB, recombinant expression in Corynebacterium glutamicum strain LYS-12, coexpression with Pseudomonas putida gene davA, encoding 5-aminovaleramidase
-
gene davB, recombinant expression in Escherichia coli strain WL3110, coexpression with gene davA, encoding 5-aminovaleramidase
-
gene davB, recombinant expression in Escherichia coli, coexpression with gene davA, encoding 5-aminovaleramidase, lysine specific permease LysP, and PP2911, a 4-aminobutyrate transporter, since Escherichia coli is unable to assimilate L-lysine and to secrete 5-aminovalerate
-
gene davB, recombinant expression in Escherichia coli, coexpression with gene davA, encoding 5-aminovaleramidase, recombinant expression of gene davB as N-terminally His-tagged enzyme in Corynebacterium glutamicum, a highly L-lysine producing strain BE using the sod promoter and the transcription factor Tu, EC 3.6.5.3
-
gene davB, recombinant expression of codon-optimized enzyme DavB in Escherichia coli strains BL21(DE3) and BL-22A-RB-YB, coexpression with gene davA, encoding 5-aminovaleramide amidohydrolase
-
gene davB, recombinant expression of His-tagged enzyme DavB in Escherichia coli, coexpression with gene davA, encoding 5-aminovaleramidase
-
gene laao/mog, recombinant expression of His-tagged wild-type enzyme L-amino acid oxidase/monooxygenase in Escherichia coli strain BL21(DE3), selenomethionine-labeled enzyme is expressed in Escherichia coli strain BL21 CodonPlus (DE3)-RIL-X
recombinantly expressed in Escherichia coli. Wild-type Escherichia coli enzyme can not convert lysine to 5-aminovalerate, whereas recombinant Escherichia coli enzyme expressing the davBA genes encoding lysine 2-monooxygenase and delta-aminovaleramidase produces 5-aminovalerate from lysine with a 64% conversion yield
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C254A
site-directed mutagenesis, the mutant shows unaltered lysine 2-monooxygenase activity compared to the wild-type
C254D
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
C254E
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
C254F
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
C254G
site-directed mutagenesis, the mutant shows slightly reduced lysine 2-monooxygenase activity compared to the wild-type
C254H
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
C254I
site-directed mutagenesis, the mutant enzyme shows 5times higher specific activity of oxidase activity compared to wild-type, while the lysine 2-monooxygenase activity is completely abolished
C254L
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type; site-directed mutagenesis, the mutant shows moderately reduced lysine 2-monooxygenase activity compared to the wild-type
C254M
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
C254N
site-directed mutagenesis, the mutant shows moderately reduced lysine 2-monooxygenase activity compared to the wild-type
C254P
site-directed mutagenesis, the mutant shows moderately reduced lysine 2-monooxygenase activity compared to the wild-type
C254Q
site-directed mutagenesis, the mutant shows moderately reduced lysine 2-monooxygenase activity compared to the wild-type
C254R
site-directed mutagenesis, the mutant shows moderately reduced lysine 2-monooxygenase activity compared to the wild-type
C254S
site-directed mutagenesis, the mutant shows slightly reduced lysine 2-monooxygenase activity compared to the wild-type
C254T
site-directed mutagenesis, the mutant shows unaltered lysine 2-monooxygenase activity compared to the wild-type
C254V
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
C254W
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type; site-directed mutagenesis, the mutant shows moderately reduced lysine 2-monooxygenase activity compared to the wild-type
C254Y
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
synthesis